AC MF_00175; DC Protein; auto TR HAMAP; MF_00175; -; 1; level=0 XX Names: ClpX XX ID CLPX DE RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX; GN Name=clpX; XX CC -!- FUNCTION: ATP-dependent specificity component of the Clp protease. It CC directs the protease to specific substrates. Can perform chaperone CC functions in the absence of ClpP. CC -!- SUBUNIT: Component of the ClpX-ClpP complex. Forms a hexameric ring CC that, in the presence of ATP, binds to fourteen ClpP subunits assembled CC into a disk-like structure with a central cavity, resembling the CC structure of eukaryotic proteasomes. CC -!- SIMILARITY: Belongs to the ClpX chaperone family. XX DR Pfam; PF00004; AAA; 1; trigger=no DR Pfam; PF06689; zf-C4_ClpX; 1; trigger=no DR NCBIfam; TIGR00382; clpX; 1; trigger=no DR PROSITE; PS51902; CLPX_ZB; 1; trigger=yes XX KW ATP-binding KW Chaperone KW Metal-binding KW Nucleotide-binding KW Zinc XX GO GO:0005524; F:ATP binding GO GO:0051082; F:unfolded protein binding GO GO:0006457; P:protein folding XX FT From: CLPX_ECOLI (P0A6H1) FT BINDING 120..127 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: [PS]-[ST]-G-x-G-K-T-[LYFV] FT BINDING 15 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 18 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 37 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 40 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C XX Size: 380-500; Related: MF_00249; Template: P0A6H1; O25926; Scope: Bacteria Fusion: Nter: None Cter: None Duplicate: in METCA, WOLSU Plasmid: None Comments: Unknown insert in BIFLO XX # Revision 1.28 2023/06/01 //